Nuclear PI5P, Uhrf1, and the road not taken

Nicolas Reynoird; Or Gozani

doi:10.1016/j.molcel.2014.06.012

Nuclear PI5P, Uhrf1, and the road not taken

Mol Cell. 2014 Jun 19;54(6):901-903. doi: 10.1016/j.molcel.2014.06.012.

Authors

Nicolas Reynoird¹, Or Gozani²

Affiliations

¹ Department of Biology, Stanford University, Stanford, CA 94305, USA.
² Department of Biology, Stanford University, Stanford, CA 94305, USA. Electronic address: ogozani@stanford.edu.

Abstract

In this issue of Molecular Cell, Gelato et al. (2014) identify the signaling molecule phosphatidylinositol 5-phosphate (PI5P) as an allosteric regulator that determines the mode of chromatin binding for the DNA methylation maintenance factor Uhrf1. This work links nuclear lipids to chromatin signaling in the maintenance of DNA methylation and epigenetic regulation.

Publication types

Comment

MeSH terms

CCAAT-Enhancer-Binding Proteins / chemistry*
Histones / chemistry*
Humans
Phosphatidylinositol Phosphates / chemistry*
Ubiquitin-Protein Ligases

Substances

CCAAT-Enhancer-Binding Proteins
Histones
Phosphatidylinositol Phosphates
phosphatidylinositol 5-phosphate
UHRF1 protein, human
Ubiquitin-Protein Ligases

Grants and funding

R01 GM079641/GM/NIGMS NIH HHS/United States